Lemon-derived carbon dots as antioxidant and light emitter in fluorescent films applied to nanothermometry.

The design of luminescent nanomaterials for the development of nanothermometers with high sensitivity and free of potentially toxic metals has developed in several fields, such as optoelectronics, sensors, and bioimaging. In addition, luminescent nanothermometers have advantages related to non-invasive measurement, with their wide detection range and high spatial resolution at the nano/microscale. Our study is the first, to our knowledge, to demonstrate a detailed study of a fluorescent film (Film-L) thermal sensor based on carbon dots derived from lemon bagasse extract (CD-L). The CD-L properties were explored as an antioxidant agent; their cytotoxicity was evaluated by using a human non-tumoral skin fibroblast (HFF-1) cell line from an MTT assay. The CD-L were characterized by HRTEM, DLS, FTIR, UV-VIS, and fluorescence spectroscopy. These confirmed their particle size distribution below 10 nm, graphitic structure in the core and surface organic groups, and strong blue emission. The CD-L showed cytocompatibility behavior and scavenging potential reactive species of biological importance: O2•- and HOCl, with IC50 of 276.8 ± 4.0 and 21.6 ± 0.7, respectively. The Film-L emission intensities (I425 nm) are temperature-dependent in the 298 to 333 K range. The Film-L luminescent thermometer shows a maximum relative thermal sensitivity of 2.69 % K-1 at 333 K.

Toxicity of thimerosal in biological systems: Conformational changes in human hemoglobin, decrease of oxygen binding capacity, increase of protein glycation and amyloid's formation.

Thimerosal (TH), an organomercurial compound, is used as a preservative in vaccines and cosmetics. Its interaction with human hemoglobin (Hb) was investigated under physiological conditions using biophysical and biological assays, aiming to evaluate hazardous effects. TH interacts spontaneously with Hb (stoichiometry 2:1, ligand-protein), preferably by electrostatic forces, with a binding constant of 1.41 × 106 M-1. Spectroscopic data allows to proposing that TH induces structural changes in Hg, through ethylmercury transfer to human Hb-Cys93 residues, forming thiosalicylic acid, which, in turn, interacts with the positive side of the amino acid in the Hb-HgEt adduct chain. As a consequence, inhibition of Hb-O2 binding capacity up to 72% (human Hb), and 50% (human erythrocytes), was verified. Dose-dependent induction of TH forming advanced glycation end products (AGE) and protein aggregates (amyloids) was additionally observed. Finally, these results highlight the toxic potential of the use of TH in biological systems, with a consequent risk to human health.